Difference between revisions of "GuaA"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2YWB 2YWB] (from ''Thermus thermophilus hb8'', 45% identity, 57% similarity) |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P29727 P29727] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P29727 P29727] |
Revision as of 11:58, 19 February 2010
- Description: GMP synthase (glutamine-hydrolysing)
Gene name | guaA |
Synonyms | guaB |
Essential | no |
Product | GMP synthetase (glutamine-hydrolysing) |
Function | biosynthesis of GMP |
Metabolic function and regulation of this protein in SubtiPathways: Purine synthesis, Nucleotides (regulation) | |
MW, pI | 57 kDa, 4.747 |
Gene length, protein length | 1539 bp, 513 aa |
Immediate neighbours | yebA, pbuG |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU06360
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 2YWB (from Thermus thermophilus hb8, 45% identity, 57% similarity)
- UniProt: P29727
- KEGG entry: [3]
- E.C. number: 6.3.5.2
Additional information
Expression and regulation
- Operon: guaA PubMed
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
P Mäntsälä, H Zalkin
Cloning and sequence of Bacillus subtilis purA and guaA, involved in the conversion of IMP to AMP and GMP.
J Bacteriol: 1992, 174(6);1883-90
[PubMed:1312531]
[WorldCat.org]
[DOI]
(P p)
H H Saxild, P Nygaard
Regulation of levels of purine biosynthetic enzymes in Bacillus subtilis: effects of changing purine nucleotide pools.
J Gen Microbiol: 1991, 137(10);2387-94
[PubMed:1722815]
[WorldCat.org]
[DOI]
(P p)